[3] Woronin bodies are present in the fungal class Pezizomycotina, which includes species such as Neurospora crassa, Aspergillus fumigatus, and various plant pathogenic fungi, like Zymoseptoria tritici.
[4] Transmission electron microscopy (TEM) reveals Woronin bodies as structures with a dense, proteinaceous core surrounded by a tightly bound unit membrane.
Evidence for this tether was strengthened by laser tweezer experiments, which demonstrated that Woronin bodies, when displaced from the septum, return to their original position upon release.
[5] One established function of Woronin bodies is the plugging of the septal pores after hyphal wounding, which restricts the loss of cytoplasm to the sites of injury.
This dynamic function enables the fungus to adapt to changing environmental conditions while maintaining cellular homeostasis by selectively regulating the flow of materials between hyphal compartments.
These loci encode the core matrix protein HEX-1, its membrane receptor WSC (Woronin sorting complex), and the cytoplasmic tether called Leashin.
These WSC, HEX-1, and Leashin proteins work together to ensure that each compartment of the fungal hypha contains tethered, immobilized Woronin bodies, ready to respond to cellular damage.
In several fungi, deletion of hex-1 leads to excessive hyphal bleeding after wounding, along with pleiotropic effects on phenotypes related to asexual reproduction, vegetative growth, and stress responses to osmotic and cell wall-perturbing agents.
Under hypotonic shock, red fluorescent Woronin bodies cluster at septal pores adjacent to lysed compartments, plugging them and preventing cytoplasmic leakage.
[21] SEM is regarded as a promising tool for analyzing fungal hyphae, allowing researchers to study cell physiology and how organelles respond to different conditions.